6uyu

X-ray diffraction
1.66Å resolution

Crystal structure of K45-acetylated SUMO1 in complex with phosphorylated PML-SIM

Released:

Function and Biology Details

Biochemical function:
  • not assigned
Biological process:
  • not assigned
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Small ubiquitin-related modifier 1 Chains: A, C
Molecule details ›
Chains: A, C
Length: 83 amino acids
Theoretical weight: 9.57 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P63165 (Residues: 17-97; Coverage: 80%)
Gene names: OK/SW-cl.43, SMT3C, SMT3H3, SUMO1, UBL1
Sequence domains: Ubiquitin-2 like Rad60 SUMO-like
Protein PML Chains: B, D
Molecule details ›
Chains: B, D
Length: 29 amino acids
Theoretical weight: 3.3 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P29590 (Residues: 547-574; Coverage: 3%)
  • Best match: P29590-8 (Residues: 547-570)
Gene names: MYL, PML, PP8675, RNF71, TRIM19

Ligands and Environments

1 bound ligand:
2 modified residues:

Experiments and Validation Details

Entry percentile scores
X-ray source: CLSI BEAMLINE 08ID-1
Spacegroup: P212121
Unit cell:
a: 38.536Å b: 63.136Å c: 91.378Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.171 0.169 0.186
Expression system: Escherichia coli